ID F2Q237_TRIEC Unreviewed; 808 AA.
AC F2Q237;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=TEQG_07263 {ECO:0000313|EMBL:EGE08205.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995774; EGE08205.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q237; -.
DR MEROPS; M03.009; -.
DR VEuPathDB; FungiDB:TEQG_07263; -.
DR eggNOG; KOG2089; Eukaryota.
DR HOGENOM; CLU_001805_1_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..604
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT DOMAIN 620..806
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 88..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 90818 MW; 4A029D9E45EA2BBA CRC64;
MAMDPILAAP LQLALTRPYY PLITVTERRV LTSAILALAT RRSVSLFLLA LPLFVVAVLI
LAPALRFPAL GLPSLRAAAR PAFVFPPSRS NSTTATSTAT STATRPTAAS FLRSTTPLTA
TSRPLTTASM APSALRSPPQ PPPLFTGTPT SVVEDTKRLI ELSRAIQDGV AKNVTAETAS
FDKVVLPLAR DENTMALESH ILGFYQSVST DSKLRDASTE AERLMNDFGI ESAMREDLYK
LVDAAVKKKE KLDPESQKLL EKEHKDYLRN GLGLPAGPKR DRFKEIKKRL SDIAIEFQKN
LNEENGGLWF TREQLAGVPE DVLSGLKKGE GENEGKLRLS FKYPDLFPTL KYAVEPETRK
AVMIANENKC NQNIPLFKET LLLRDEAARL LGYPNHAAFR LEDKMAKNPE TVDTFLGDLR
SRLTDGGKQE IKTLMEMKKK DIEAQKKAFD GHYFLWDHRF YDRMMLEKDY SLDHQLIAEY
FPLQTTIRGM LEIFEQIFGL VFVEIKGEER AKISSSGKGE DIVWHEDVQV FSVWNDEGEG
SGFVGYLYLD LFPREGKYGH AANFNLQPGF IKEDGSRRYP ATALVCNFSK PTEKKPSLLK
HDEVPDAREL VLDSLPTQVA SKHYSTISPE YYKAWKEHAG DKPDPAAEIP DELIQNLIKT
KHVNAALFNL RQLHFGIFDM TVHEPKDHEA IKDMNVSETY NKLRKEIASL DGPEVLGQGY
SWGHGEATFG HLMGGYDAGY YGYLSSQVYS TDMFYTVFKD DPMNKKEGRR YRYSVLEKGG
SQDEMTTLKE FLGREPKPDA FYKELGLA
//
